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Q9EVG6 (LEU3_BUCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3-isopropylmalate dehydrogenase
EC=1.1.1.85
Alternative name(s):
3-IPM-DH
Beta-IPM dehydrogenase
Short name=IMDH
Gene names
Name:leuB
Encoded onPlasmid pLeu (pBAp1)
OrganismBuchnera aphidicola subsp. Uroleucon aeneum
Taxonomic identifier118112 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. HAMAP MF_01033

Catalytic activity

(2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH. HAMAP MF_01033

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. HAMAP MF_01033

Subunit structure

Homodimer By similarity. HAMAP MF_01033

Subcellular location

Cytoplasm By similarity HAMAP MF_01033.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Branched-chain amino acid biosynthesis
Leucine biosynthesis
   Cellular componentCytoplasm
   LigandMagnesium
Manganese
Metal-binding
NAD
   Molecular functionOxidoreductase
   Technical termPlasmid
Gene Ontology (GO)
   Biological processleucine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-isopropylmalate dehydrogenase activity

Inferred from electronic annotation. Source: EC

NAD binding

Inferred from electronic annotation. Source: InterPro

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3633633-isopropylmalate dehydrogenase HAMAP MF_01033
PRO_0000083663

Regions

Nucleotide binding78 – 9114NAD By similarity
Nucleotide binding285 – 29713NAD By similarity

Sites

Metal binding2271Magnesium or manganese By similarity
Metal binding2511Magnesium or manganese By similarity
Metal binding2551Magnesium or manganese By similarity
Binding site991Substrate By similarity
Binding site1091Substrate By similarity
Binding site1381Substrate By similarity
Binding site2271Substrate By similarity
Site1451Important for catalysis By similarity
Site1951Important for catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9EVG6 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 15E972DAABFE6996

FASTA36340,524
        10         20         30         40         50         60 
MTRKYRIAVL PGDGIGPEVM REAYKILNIL KDDFSLPLEI KEFNIGGAAI DQEGVALPKK 

        70         80         90        100        110        120 
TLLGCENSDA ILFGSVGGKK WDNLPINQRP ERASLLPLRK HFNLFANLRP AQLYSELKNL 

       130        140        150        160        170        180 
SPLRSNIIKN GFNILCIREL TGGIYFGKPT GRLKKNNIEY AFDTEIYYNY EINRIAHLAF 

       190        200        210        220        230        240 
QLSQTRNYKV CSIDKSNVLN SSILWREIVK KVSKHYPDVH LSHLYIDNAT MQIIKDPNQF 

       250        260        270        280        290        300 
DVLLCSNLFG DIISDECAMI TGSIGMLPSA SLNEKKFGLY EPAGGSAPDI EGKNIANPIA 

       310        320        330        340        350        360 
QILSLSMLVR YSMNLKKIAD KIDQSVISVL KKGYRTADIS NNNDYLKTNE MGDVIASALI 


SGE

« Hide

References

[1]"Vertical transmission of biosynthetic plasmids in aphid endosymbionts (Buchnera)."
Wernegreen J.J., Moran N.A.
J. Bacteriol. 183:785-790(2001) [PubMed: 11133977] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF197455 Genomic DNA. Translation: AAG31399.1.

3D structure databases

ProteinModelPortalQ9EVG6.
SMRQ9EVG6. Positions 1-362.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01033. LeuB_type1.
[Tree]
InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
IPR004429. Isopropylmalate_DH.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHERPTHR11835. IDH_IMDH_dimeric. 1 hit.
PTHR11835:SF13. IPMDH. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00169. LeuB. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEU3_BUCUA
AccessionPrimary (citable) accession number: Q9EVG6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: March 1, 2001
Last modified: July 27, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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